Fractal Analysis of Aggregates Formed by Heating Dilute BSA Solutions Using Light Scattering Methods

Hagiwara, Takaaki; Kumagai, Hitoshi; Nakamura, Kozo

doi:10.1271/bbb.60.1757

Cited by 58 publications

(36 citation statements)

References 14 publications

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“…A similar trend has been found for numerous other proteins [30][31][32]. At pH values close to neutral, the aggregation of BSA is reaction controlled whereas it becomes faster and diffusion controlled if pH is lowered towards pI, which is ~5 [17,18]. …”

Section: Discussionsupporting

confidence: 74%

“…At neutral pH, the irreversible step for the thermal denaturation of BSA controlled by the formation of soluble "β-aggregates" in which a moderate part of the native helices are converted into intermolecular β-sheets which connect the protein monomers [17]. Under these conditions the aggregates are small, without pronounced polydispersity and their growth is governed by a reaction-limited mechanism [17][18][19]. These properties make BSA an adequate model system for studies of solute effects on irreversible transitions.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

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Solute effects on the irreversible aggregation of serum albumin

Bagger¹,

Ōgendal²,

Westh³

2007

Biophysical Chemistry

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT2 AbstractThermal stress on bovine serum albumin (BSA) promotes protein aggregation through the formation of intermolecular β-sheets. We have used light scattering and chromatography to study effects of (<1M) Na 2 SO 4 , NaSCN, sucrose, sorbitol and urea on the rate of the thermal aggregation. Both salts were strong inhibitors of BSA-aggregation and they reduced both the size and number (concentration) of aggregate particles compared to non-ionic solutes (or pure buffer). Hence, the salts appear to suppress both nucleation-and growth rate. The nonelectrolyte additives reduced the initial aggregation rate (compared to pure buffer), but did not significantly limit the extent of aggregation in samples quenched after 27 min. heat exposure

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Section: Discussionsupporting

confidence: 74%

Section: Accepted Manuscriptmentioning

confidence: 99%

Solute effects on the irreversible aggregation of serum albumin

Bagger¹,

Ōgendal²,

Westh³

2007

Biophysical Chemistry

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show abstract

“…Light scattering has proven to be a powerful technique for such a characterisation. It was shown with this technique that globular proteins such as bovum serum albumin (BSA) [3], ovalbumin (OA) [4] and ␤-lactoglobulin (␤-lg) [5][6][7] form self similar aggregates characterised by a fractal dimension. Of these proteins ␤-lg is probably the best characterised, but even for this protein no systematic study was made of the structure of the aggregates as a function of the ionic strength.…”

Section: Introductionmentioning

confidence: 99%

Influence of the ionic strength on the heat-induced aggregation of the globular protein β-lactoglobulin at pH 7

Baussay

Bon

Nicolai

et al. 2004

International Journal of Biological Macromolecules

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“…9 11) Shih et al evaluated the fractal dimension of boehmite alumina col1oidal gels from the measurement of the elasticity of the gels, using a theory different from that of Bremer et al 12) We have shown that the value of the fractal dimensions of the aggregates formed by heating dilute bovine serum albumin (BSA) solutions was 1.8 or 2.1 with light scattering methods, being close to those predicted by the cluster-cluster aggregation model. 13) We have also done fractal analysis t To whom correspondence should be addressed.…”

mentioning

confidence: 99%